GenomeNet

Database: UniProt
Entry: A0A0N0J627_9PROT
LinkDB: A0A0N0J627_9PROT
Original site: A0A0N0J627_9PROT 
ID   A0A0N0J627_9PROT        Unreviewed;       939 AA.
AC   A0A0N0J627;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Phosphoenolpyruvate carboxylase {ECO:0000256|ARBA:ARBA00022419, ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPC {ECO:0000256|HAMAP-Rule:MF_00595};
DE            Short=PEPCase {ECO:0000256|HAMAP-Rule:MF_00595};
DE            EC=4.1.1.31 {ECO:0000256|ARBA:ARBA00012305, ECO:0000256|HAMAP-Rule:MF_00595};
GN   Name=ppc {ECO:0000256|HAMAP-Rule:MF_00595};
GN   ORFNames=IP80_20125 {ECO:0000313|EMBL:KPF42797.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF42797.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF42797.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF42797.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Forms oxaloacetate, a four-carbon dicarboxylic acid source
CC       for the tricarboxylic acid cycle. {ECO:0000256|ARBA:ARBA00003670,
CC       ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=oxaloacetate + phosphate = hydrogencarbonate +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31;
CC         Evidence={ECO:0000256|ARBA:ARBA00001071, ECO:0000256|HAMAP-
CC         Rule:MF_00595};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00595};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- SIMILARITY: Belongs to the PEPCase type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008346, ECO:0000256|HAMAP-Rule:MF_00595}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KPF42797.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJHW01000054; KPF42797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0J627; -.
DR   STRING; 1523424.IP80_20125; -.
DR   PATRIC; fig|1523424.3.peg.3527; -.
DR   Proteomes; UP000037849; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008964; F:phosphoenolpyruvate carboxylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006107; P:oxaloacetate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   Gene3D; 1.20.1440.90; Phosphoenolpyruvate/pyruvate domain; 1.
DR   HAMAP; MF_00595; PEPcase_type1; 1.
DR   InterPro; IPR021135; PEP_COase.
DR   InterPro; IPR022805; PEP_COase_bac/pln-type.
DR   InterPro; IPR018129; PEP_COase_Lys_AS.
DR   InterPro; IPR033129; PEPCASE_His_AS.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   PANTHER; PTHR30523; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   PANTHER; PTHR30523:SF6; PHOSPHOENOLPYRUVATE CARBOXYLASE; 1.
DR   Pfam; PF00311; PEPcase; 1.
DR   PRINTS; PR00150; PEPCARBXLASE.
DR   SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR   PROSITE; PS00781; PEPCASE_1; 1.
DR   PROSITE; PS00393; PEPCASE_2; 1.
PE   3: Inferred from homology;
KW   Carbon dioxide fixation {ECO:0000256|ARBA:ARBA00023300, ECO:0000256|HAMAP-
KW   Rule:MF_00595};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00595};
KW   Pyruvate {ECO:0000313|EMBL:KPF42797.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037849}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        160
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10111"
FT   ACT_SITE        589
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00595,
FT                   ECO:0000256|PROSITE-ProRule:PRU10112"
SQ   SEQUENCE   939 AA;  103844 MW;  DC9B543D84708490 CRC64;
     MKTASASTRT RTKTASDDAA AKNKPLVEDI RLLGRILGDV IREQEGTAAF ELIERVRQLS
     VAYRLKADAS AGRVLDRLLK NLSADQTVTV IRAFSYFSHL ANIAEDRHHV RRRSVHERAG
     DLQEGSLALS FERLQRADHR AADIAATLHG AYISPVLTAH PTEVQRKSIL DAERAVAELL
     EQRDELPTEE RRAENEALMR ARVTQLWQTR MLRTAKLTVA DEIENALSYY GTTFLREIPR
     LYRDVERALP GHAVGNFLRM GHWIGGDRDG NPNVTAATLA HALKRQAEVA LRFYLTEVHE
     LGAELSISGT LAPVSPEMQA LAAASPDSNP HRLDEPYRRA LIGMYSRLAA TLQALTGTEA
     LRHAVAPQNP YPGPEAFLAD LRTIERSLGS HHAQALVGPR LAPLMRAVQV FGFHLATLDL
     RQSSDKHEAV VAELLRVARI EADYSALSEP QRRTCLLALL NDARPLRVHG SPYSPLALDE
     LAIFETAREA LTRYGAQTLR HCIISHTEEV SDLLEVLLLQ KEAGLLTGTL DQPGTKAALI
     TVPLFETIGD LRRSEPIMRE FYALPGVHAL VRNSGAEQDV MLGYSDSNKD GGSFTSHWEL
     FRAETALAAL FAELNAAQAR SKPITLRLFH GRGGTVGRGG GPSYQAILAQ PPGTVNGQIR
     LTEQGEVIAS KYANPEIGRR NLETLVAATL EATMLHPTKP APKAFLDAAA EISEASFQAY
     RQLVYGTPGF TDYFFAATPI REIAELNIGS RPASRKATRA IEDLRAIPWS FSWGQCRMAL
     PGWCGFGSAI EAFLAQGDRA ERAALLQRMH KQWPFFRTLL SNLDMVLAKS DLRIAARYVE
     LVEDKKVAKR IFGLLKAEWQ RASEALTLIT GQQQPLQGNP ALARSIAHRF PYLDPLNHLQ
     VELMRRYRTR REGQEGVERL QRGIHLSING IAAGLRNTG
//
DBGET integrated database retrieval system